DUSP2: Difference between revisions
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| | '''Dual specificity protein phosphatase 2''' is an [[enzyme]] that in humans is encoded by the ''DUSP2'' [[gene]].<ref name="pmid7806236">{{cite journal | vauthors = Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM | title = Chromosomal localization of four human VH1-like protein-tyrosine phosphatases | journal = Genomics | volume = 22 | issue = 2 | pages = 462–4 |date=Jan 1995 | pmid = 7806236 | pmc = | doi = 10.1006/geno.1994.1411 }}</ref><ref name="pmid7590752">{{cite journal | vauthors = Yi H, Morton CC, Weremowicz S, McBride OW, Kelly K | title = Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11 | journal = Genomics | volume = 28 | issue = 1 | pages = 92–6 |date=Dec 1995 | pmid = 7590752 | pmc = | doi = 10.1006/geno.1995.1110 }}</ref><ref name="pmid12673251">{{cite journal | vauthors = Yin Y, Liu YX, Jin YJ, Hall EJ, Barrett JC | title = PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression | journal = Nature | volume = 422 | issue = 6931 | pages = 527–31 |date=Apr 2003 | pmid = 12673251 | pmc = | doi = 10.1038/nature01519 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DUSP2 dual specificity phosphatase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1844| accessdate = }}</ref> | ||
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| summary_text = The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.<ref name="entrez" | | summary_text = The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.<ref name="entrez" /> | ||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Wu J, Jin YJ, Calaf GM |title=PAC1 is a direct transcription target of E2F-1 in apoptotic signaling |journal=Oncogene |volume=26 |issue= 45 |pages= 6526–35 |year= 2007 |pmid= 17471234 |doi= 10.1038/sj.onc.1210484 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Zhang Q, Muller M, Chen CH |title=New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding |journal=J. Mol. Biol. |volume=354 |issue= 4 |pages= 777–88 |year= 2006 |pmid= 16288922 |doi= 10.1016/j.jmb.2005.10.006 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kothapalli R, Yoder SJ, Kusmartseva I, Loughran TP |title=Characterization of a variant of PAC-1 in large granular lymphocyte leukemia |journal=Protein Expr. Purif. |volume=32 |issue= 1 |pages= 52–60 |year= 2004 |pmid= 14680939 |doi= 10.1016/S1046-5928(03)00237-7 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Zhang Y, Guan DL, Xia CQ |title=Relationship between the expression levels of CD61, CD63, and PAC-1 on platelet surface in peripheral blood and the transplanted kidney function |journal=Transplant. Proc. |volume=35 |issue= 4 |pages= 1360–3 |year= 2004 |pmid= 12826159 |doi=10.1016/S0041-1345(03)00469-X |display-authors=etal}} | ||
*{{cite journal | vauthors=Farooq A, Plotnikova O, Chaturvedi G |title=Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP |journal=Structure |volume=11 |issue= 2 |pages= 155–64 |year= 2003 |pmid= 12575935 |doi=10.1016/S0969-2126(02)00943-7 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ward Y, Gupta S, Jensen P |title=Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1 |journal=Nature |volume=367 |issue= 6464 |pages= 651–4 |year= 1994 |pmid= 8107850 |doi= 10.1038/367651a0 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Rohan PJ, Davis P, Moskaluk CA |title=PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase |journal=Science |volume=259 |issue= 5102 |pages= 1763–6 |year= 1993 |pmid= 7681221 |doi=10.1126/science.7681221 |display-authors=etal}} | ||
*{{cite journal | vauthors=Raingeaud J, Gupta S, Rogers JS |title=Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7420–6 |year= 1995 |pmid= 7535770 |doi=10.1074/jbc.270.13.7420 |display-authors=etal}} | |||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=1844}} | |||
{{Protein tyrosine phosphatases}} | |||
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Latest revision as of 18:45, 30 August 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
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Location (UCSC) | n/a | n/a | |||||
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Dual specificity protein phosphatase 2 is an enzyme that in humans is encoded by the DUSP2 gene.[1][2][3][4]
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.[4]
References
- ↑ Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM (Jan 1995). "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases". Genomics. 22 (2): 462–4. doi:10.1006/geno.1994.1411. PMID 7806236.
- ↑ Yi H, Morton CC, Weremowicz S, McBride OW, Kelly K (Dec 1995). "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11". Genomics. 28 (1): 92–6. doi:10.1006/geno.1995.1110. PMID 7590752.
- ↑ Yin Y, Liu YX, Jin YJ, Hall EJ, Barrett JC (Apr 2003). "PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression". Nature. 422 (6931): 527–31. doi:10.1038/nature01519. PMID 12673251.
- ↑ 4.0 4.1 "Entrez Gene: DUSP2 dual specificity phosphatase 2".
Further reading
- Wu J, Jin YJ, Calaf GM, et al. (2007). "PAC1 is a direct transcription target of E2F-1 in apoptotic signaling". Oncogene. 26 (45): 6526–35. doi:10.1038/sj.onc.1210484. PMID 17471234.
- Zhang Q, Muller M, Chen CH, et al. (2006). "New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding". J. Mol. Biol. 354 (4): 777–88. doi:10.1016/j.jmb.2005.10.006. PMID 16288922.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Kothapalli R, Yoder SJ, Kusmartseva I, Loughran TP (2004). "Characterization of a variant of PAC-1 in large granular lymphocyte leukemia". Protein Expr. Purif. 32 (1): 52–60. doi:10.1016/S1046-5928(03)00237-7. PMID 14680939.
- Zhang Y, Guan DL, Xia CQ, et al. (2004). "Relationship between the expression levels of CD61, CD63, and PAC-1 on platelet surface in peripheral blood and the transplanted kidney function". Transplant. Proc. 35 (4): 1360–3. doi:10.1016/S0041-1345(03)00469-X. PMID 12826159.
- Farooq A, Plotnikova O, Chaturvedi G, et al. (2003). "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP". Structure. 11 (2): 155–64. doi:10.1016/S0969-2126(02)00943-7. PMID 12575935.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ward Y, Gupta S, Jensen P, et al. (1994). "Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1". Nature. 367 (6464): 651–4. doi:10.1038/367651a0. PMID 8107850.
- Rohan PJ, Davis P, Moskaluk CA, et al. (1993). "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase". Science. 259 (5102): 1763–6. doi:10.1126/science.7681221. PMID 7681221.
- Raingeaud J, Gupta S, Rogers JS, et al. (1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. 270 (13): 7420–6. doi:10.1074/jbc.270.13.7420. PMID 7535770.
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